ProblemSet7AK - 1. An apoenzyme requires a -(cofactor) to...

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1. An apoenzyme requires a ---(cofactor) to become a holoenzyme. 2. The class of metals whose ions most frequently function as enzyme cofactors is the ---(transition metal). 3. The rate enhancement ( ' / G RT e ° ) you could expect from the catalytic effect of a 15 kJ/mol hydrogen bond at 25°C would be (424)______ times. 4. Proteolytic enzymes don't digest the pancreas, where they are synthesized, because they are in the (Zymogen)______ form until they enter the digestive tract. 5. Fe 2+ is not classified as a coenzyme because coenzymes are usually (small organic compounds)______. 6. In addition to proteins, certain (RNA)______ molecules have been found to possess enzymatic activity. 7. TPP (thiamine pyrophosphate) is an example of a (coenzyme)______ acting as a covalent catalyst. 8. (Elastase)_____ is a serine protease that recognizes residues with small neutral side chains. 9. Which of these amino acid groups would not make a good nucleophilic catalyst? A) amino B) sulfhydryl C) imidazole D) Methyl X E) hydroxyl 10. Chymotrypsin, a serine protease, preferentially cleaves a peptide bond adjoining a bulky non-polar side chain. This is because chymotrypsin's “specificity pocket”: A) contains a sulfhydryl group that forms a disulfide bond with the substrate. B)
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ProblemSet7AK - 1. An apoenzyme requires a -(cofactor) to...

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